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Dongping Zhong received his B.S. in laser physics from Huazhong University of Science and Technology (China) and his Ph.D. in Chemistry from California Institute of Technology in 1999 under Prof. Ahmed H. Zewail. For his Ph.D. work, Dr. Zhong received The Herbert Newby McCoy Award and the Milton and Francis Clauser Doctoral Prize from Caltech. He continued his postdoctoral research in the same group with focus on protein dynamics. In 2002, he joined The Ohio State University as an Assistant Professor and currently he is Robert Smith Professor of Physics and Professor of Chemistry and Biochemistry. He is the Packard Fellow, Sloan Fellow, Camille Dreyfus Teacher-Scholar as well as the recipient of the NSF CAREER award. His research interests include biomolecular interactions and ultrafast protein dynamics.
Femtobiology, Biomolecular Interactions, Protein Dynamics
Research in the Zhong group is directed towards understanding the nature of elementary processes in biological systems. We relate dynamics and structures to functions at the most fundamental level with state-of-the-art femtosecond lasers and molecular biology methods. The laboratory ultimately will have the capability of time resolution from femtosecond to millisecond (second); biological systems can be prepared and studied at the single molecule level. We are currently focusing on studies of molecular recognition and ultrafast protein dynamics of several important biological systems.
- Molecular Recognition. Biomolecular recognition is governed by physical forces and the understanding of electrostatic interactions at the atomic scale is fundamental to protein science. We are particularly interested in protein-DNA/ligand/protein binding processes and study local hydration, complex rigidity and conformation dynamics. Intrinsic amino acid residue tryptophan has been characterized in various biological environments to probe electrostatic interactions; several important resonance energy transfer pairs have been developed to study conformational changes. Molecular mutation is used to investigate site-specific interactions. These studies are important to drug transport and design, protein folding and unfolding, and enzyme catalysis.
- Ultrafast Protein Dynamics. A variety of ultrafast elementary reactions involved in protein functioning such as twist motion, proton, electron and energy transfer, and bond breaking and making will be studied. Site-direct mutagenesis will be used to alter structurally and chemically important residue(s) to study the local reactivity. These studies will elucidate the role of dynamics in structure-dynamics-function correlation and the nature of non-equilibrium biological dynamics by coherent femtosecond laser preparation. Currently, we focus on DNA-repair enzymes (photolyases) to map out the entire evolution of functional processes and thus reveal the molecular mechanism of this important biological function. A similar photosensory protein (cryptochrome) is also being studied to elucidate its key photochemistry for synchronization of biological timing (circadian rhythm).
The cutting-edge interdisciplinary research in the Zhong group is currently supported by the National Science Foundation (NSF), the National Institute of Health (NIH) and various private Foundations. The former members of the Zhong group currently hold post-doctoral positions in Harvard, Princeton, Columbia, Cornell and ETH, and faculty positions in US, India and China. The Zhong group always has positions open for committed students and welcomes discussion of interests in his group.
J. Li, Z. Liu, C. Tan, X. Guo, L. Wang, A. Sancar and D. Zhong, Nature 466, 887 (2010). Dynamics and mechanism of repair of ultraviolet-induced (6-4) photoproduct by photolyase.
C.-W. Chang, L. Guo, Y.-T. Kao, J. Li, C. Tan, T. Li, C. Saxena, Z. Liu, L. Wang, A. Sancar and D. Zhong, Proc. Natl. Acad. Sci. USA 107, 2914 (2010). Ultrafast solvation dynamics at binding and active sites of photolyases.
J. A. Stevens, J. J. Link, Y.-T. Kao, C. Zang, L. Wang and D. Zhong, J. Phys. Chem. B 114, 1498 (2010). Ultrafast dynamics of resonance energy transfer in myoglobin: Probing local conformation fluctuations.
L. Zhang, Y. Yang, Y.-T. Kao, L. Wang and D. Zhong, J. Am. Chem. Soc. 131, 10677 (2009). Protein hydration dynamics and molecular mechanism of coupled water-protein fluctuations.
D. Zhong, Adv. Chem. Phys. 143, 83 (2009). (Invited review). Hydration dynamics and coupled water-protein fluctuations probed by intrinsic tryptophan.
C. Zang, J. A. Stevens, J. J. Link, L. Guo, L. Wang and D. Zhong, J. Am. Chem. Soc. 131, 2846 (2009). Ultrafast proteinquake dynamics in cytochrome c.